+Open data
-Basic information
Entry | Database: PDB / ID: 3hkm | ||||||
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Title | Crystal Structure of rice(Oryza sativa) Rrp46 | ||||||
Components | Os03g0854200 protein | ||||||
Keywords | HYDROLASE / RNase PH domain / PHOSPHORYLASE | ||||||
Function / homology | Function and homology information cytoplasmic exosome (RNase complex) / U4 snRNA 3'-end processing / : / DNA nuclease activity / poly(A)-dependent snoRNA 3'-end processing / nuclear exosome (RNase complex) / rRNA catabolic process / nuclear mRNA surveillance / exonuclease activity / RNA nuclease activity ...cytoplasmic exosome (RNase complex) / U4 snRNA 3'-end processing / : / DNA nuclease activity / poly(A)-dependent snoRNA 3'-end processing / nuclear exosome (RNase complex) / rRNA catabolic process / nuclear mRNA surveillance / exonuclease activity / RNA nuclease activity / rRNA processing / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / double-stranded DNA binding / single-stranded RNA binding / nucleolus / identical protein binding Similarity search - Function | ||||||
Biological species | Oryza sativa Japonica Group (Japanese rice) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9845 Å | ||||||
Authors | Yang, C.-C. / Wang, Y.-T. / Hsiao, Y.-Y. / Doudeva, L.G. / Yuan, H.S. | ||||||
Citation | Journal: Rna / Year: 2010 Title: Structural and biochemical characterization of CRN-5 and Rrp46: an exosome component participating in apoptotic DNA degradation Authors: Yang, C.-C. / Wang, Y.-T. / Hsiao, Y.-Y. / Doudeva, L.G. / Kuo, P.-H. / Chow, S.Y. / Yuan, H.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3hkm.cif.gz | 135.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3hkm.ent.gz | 105.8 KB | Display | PDB format |
PDBx/mmJSON format | 3hkm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hk/3hkm ftp://data.pdbj.org/pub/pdb/validation_reports/hk/3hkm | HTTPS FTP |
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-Related structure data
Related structure data | 3krnC 2nn6S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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Details | DIMER DISSOCIATED INTO MONOMERS IN REMARK 350 THE CRYSTALLIZATION CONDITION |
-Components
#1: Protein | Mass: 27012.609 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryza sativa Japonica Group (Japanese rice) Strain: Japonica Group / Gene: putative exonuclease RRP46 / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(RIPL) References: UniProt: Q84T68, Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 51.96 % Description: The original data was scaled to 2.0 Angstrom by HKL2000. Then refinement was performed with all scaled data automatically by phenix.refine. The highest resolution of 1.98A was made by phenix.refine. |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.2M sodium malonate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: BL13C1 / Wavelength: 1 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jun 15, 2008 |
Radiation | Monochromator: Si 111 chnnel / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection twin | Operator: h,-h-k,-l / Fraction: 0.501 |
Reflection | Resolution: 1.98→50 Å / Num. obs: 55506 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.34 % / Rmerge(I) obs: 0.057 / Rsym value: 0.065 / Net I/σ(I): 21.65 / Num. measured all: 185470 |
Reflection shell | Resolution: 1.98→2.07 Å / Redundancy: 3 % / Rmerge(I) obs: 0.381 / Mean I/σ(I) obs: 3.15 / Num. unique all: 5536 / Rsym value: 0.354 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 2NN6 chain D Resolution: 1.9845→26.807 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.835 / Isotropic thermal model: isotropic / σ(F): 0.12 / Phase error: 24.27 / Stereochemistry target values: TWIN_LSQ_F
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 51.857 Å2 / ksol: 0.349 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 45.5 Å2 / Biso mean: 26.089 Å2 / Biso min: 13.88 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9845→26.807 Å
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Refine LS restraints |
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LS refinement shell |
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